Document Detail

Purification and enzymatic properties of a peroxidase from leaves of Phytolacca dioica L. (Ombú tree).
MedLine Citation:
PMID:  21266109     Owner:  NLM     Status:  In-Data-Review    
A peroxidase (PD-cP; 0.47 mg/100 g leaves) was purified from autumn leaves of Phytolacca dioica L. and characterized. PD-cP was obtained by acid precipitation followed by gel-filtration and cation exchange chromatography. Amino acid composition and N-terminal sequence of PD-cP up to residue 15 were similar to that of Spinacia oleracea (N-terminal pairwise comparison showing four amino acid differences). PD-cP showed a molecular mass of approx. 36 kDa by SDS-PAGE, pH and temperature optima at 3.0 and 50.0°C, respectively and seasonal variation. The Michaelis-Menten constant (K(M)) for H(2)O(2) was 5.27 mM, and the velocity maximum (V(max)) 1.31 nmol min(-1), while the enzyme turnover was 0.148 s(-1). Finally, the presence of Ca(2+) and Mg(2+) enhanced the PD-cP activity, with Mg(2+) 1.4-fold more effective than Ca(2+) [BMB reports 2011; 44(1): 64-69].
Vincenzo Guida; Giovanna Criscuolo; Rachele Tamburino; Livia Malorni; Augusto Parente; Antimo Di Maro
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  BMB reports     Volume:  44     ISSN:  1976-670X     ISO Abbreviation:  BMB Rep     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2011-01-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101465334     Medline TA:  BMB Rep     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  64-9     Citation Subset:  IM    
Dipartimento di Scienze della Vita, Seconda Universitá di Napoli, I-81100 Caserta, Italy
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